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Allostery in the Hsp70 chaperone proteins

Heat shock 70 kDa (Hsp70) chaperones are essential to in-vivo protein folding, protein transport and protein re-folding. They carry out these activities using repeated cycles of binding and release of client proteins. This process is under allosteric control of nucleotide binding and hydrolysis. X-r...

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Hlavní autoři: Zuiderweg, Erik R.P., Bertelsen, Eric B., Rousaki, Aikaterini, Mayer, Matthias P., Gestwicki, Jason E., Ahmad, Atta
Médium: Artigo
Jazyk:Inglês
Vydáno: 2013
Témata:
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC3623542/
https://ncbi.nlm.nih.gov/pubmed/22576356
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1007/128_2012_323
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